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Different roles of the two high-oxygen-affinity terminal oxidases of Brucella suis: Cytochrome c oxidase, but not ubiquinol oxidase, is required for persistence in mice.
Journal article   Peer reviewed

Different roles of the two high-oxygen-affinity terminal oxidases of Brucella suis: Cytochrome c oxidase, but not ubiquinol oxidase, is required for persistence in mice.

Maria Pilar Jiménez de Bagüés, Séverine Loisel-Meyer, Jean-Pierre Liautard and Véronique Jubier-Maurin
Infection and Immunity, Vol.75(1), pp.531-5
01/2007
PMCID: PMC1828397
PMID: 17101669

Abstract

Animals Brucella suis Brucellosis Disease Models, Animal Electron Transport Complex IV Macrophages Mice Mice, Inbred BALB C Oxidoreductases
The survival of Brucella suis mutant strains in mice demonstrated different roles of the two high-oxygen-affinity terminal oxidases. The cbb3-type cytochrome c oxidase was essential for chronic infection in oxygen-deficient organs. Lack of the cytochrome bd ubiquinol oxidase led to hypervirulence of bacteria, which could rely on nitrite accumulation inhibiting the inducible nitric oxide synthase of the host.
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